RRC ID 36278
著者 Wang H, Kiuchi T, Katsuma S, Shimada T.
タイトル A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose.
ジャーナル Insect Biochem Mol Biol
Abstract Although membrane-associated sucrase activity has been detected in the midgut of various lepidopteran species, it has not yet been identified and characterized at the molecular level. In the present study, we identified a novel sucrose hydrolase (SUH) gene from the following three bombycoid silkworms: Bombyx mori, Trilocha varians, and Samia cynthia ricini and named them BmSuh, TvSuh, and ScSuh, respectively. The EST dataset showed that BmSuh is one of the major glycoside hydrolase genes in the larval midgut of B. mori. These genes were almost exclusively expressed in the larval midgut in all three species, mainly at the feeding stage. SUHs are classified into the glycoside hydrolase family 13 and show significant homology to insect maltases. Enzymatic assays revealed that recombinant SUHs were distinct from conventional maltases and exhibited substrate specificity for sucrose. The recombinant BmSUH was less sensitive to sugar-mimic alkaloids than TvSUH and ScSUH, which may explain the reason why the sucrase activity in the B. mori midgut was less affected by the sugar-mimic alkaloids derived from mulberry.
巻・号 61
ページ 46-52
公開日 2015-6-1
DOI 10.1016/j.ibmb.2015.04.005
PII S0965-1748(15)00072-7
PMID 25937576
MeSH Alkaloids / pharmacology Animals Bombyx / drug effects Bombyx / enzymology Bombyx / genetics Gastrointestinal Tract / enzymology Glycoside Hydrolases / genetics Glycoside Hydrolases / metabolism* Insect Proteins / genetics Insect Proteins / metabolism* Larva / enzymology Larva / genetics Morus / chemistry Morus / classification Moths / drug effects Moths / enzymology* Moths / genetics* Species Specificity Substrate Specificity Sucrose / metabolism*
IF 3.827
引用数 10
WOS 分野 ENTOMOLOGY BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
カイコ p50 T. varians S. c. ricini